ID A0A0B4IKA8_METMF Unreviewed; 1162 AA.
AC A0A0B4IKA8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=SNF2-related protein {ECO:0000313|EMBL:KIE03910.1};
DE Flags: Fragment;
GN ORFNames=MAJ_00441 {ECO:0000313|EMBL:KIE03910.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE03910.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KIE03910.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE03910.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE03910.1}.
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DR EMBL; AZNE01000001; KIE03910.1; -; Genomic_DNA.
DR RefSeq; XP_014582903.1; XM_014727417.1.
DR AlphaFoldDB; A0A0B4IKA8; -.
DR HOGENOM; CLU_000315_7_0_1; -.
DR OrthoDB; 5488252at2759; -.
DR Proteomes; UP000031176; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd22254; CSB_WHD; 1.
DR CDD; cd18000; DEXHc_ERCC6; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000031176}.
FT DOMAIN 407..595
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 736..893
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIE03910.1"
SQ SEQUENCE 1162 AA; 131257 MW; A2FC23415552AFAC CRC64;
MDRDWEQEQS ADGEGGEHLV EKMIAAAQEA MHTEQTAERP ESEVMTEEDA LKKLTGTVRD
QDDLERDITI QASAALMEAE DKKDQNRMAK LDATRQRLQS QLDKEKRRLE RVAGNPYQSR
NVQKEIAKLE EELGQITGDI ADFQARIDKR HQENQLDTST HSKSKRLAGE SHREYLIRTG
KITPFAKVGG ARPEGIAGQL ADTILEAEEE AAAEQYDQEA EGPTSHQLLR RPGFIDDVVV
KDIKPSEYTV ESEFSLRPRK KRRTERERSS SADFEPDHPS GSESADSTVW QQGNEDDLIR
RENRKQKAKL RAQEQEEVDL SKLDDGNEKL YKRRLKDWIL RRSRARRARR QMADNEHTSA
ESDEDEDEWL KPSPDYPDHY INDELKLPGD IHPSLFGYQK TGVQWLAELY KQNVGGIIGD
EMGLGKTVQL IAFIAALHHS KMLERPVIVV APATLLRQWV SEFHRWWPPL RVSILHSSGS
GMMNPQFEDD YDVEHYRPVA NRSLNAARSI VRRVVDKGHV LVTTYTGLQT YADELLPVEW
GYAVLDEGHK IRNPNAEITV TCKELNTPNR VILSGTPVQN NLTELWSLFD FIYPMRLGTL
VNFRTQFEIP IRQGGYANAS NLQVMTAEKC AEALKETISE YLLQRLKIDV AADLPEKTEQ
VLFCKLTEGQ RKAYETFLGS DEVSAILNRR RQSLYGIDVL RKICNHPDLL DKSLGSKTGY
NFGSPKLSAK LELTKDLLQK VMIPNGHKTL LFSQGKLMLN IIEKCMRECN ISYLRLDGET
PVDQRQPMID RFNTDLSIHV FLMTTRTGGL GTNLTGADRI IIFDPDWNPS TDLQARERAW
RLGQNKPVKI YRLMTEGTIE EKIYHRQIFK QFMTNKVLKD PKQRSSYDLS DLYDLFSYNA
GDQAAAQRSD VFKGAEVDIS ANTDGEAVAR QRLAPITSVG HKEGDVEQEE LSKMRIVAAM
EDFQEDDSAH DERRMLEGIF SRSVNSAYDH EQIVNGPQKA KADIRVLRQE ANQVAREAAA
HLRHAAQEAR RVPIGTVTWT GEVGSGGRPG GSRRRGGPSS AGIMSNLANR QGLDGGSGSS
SRSGTPGLDR NLKAKDFVTM IKAFINRQGG RVPSKMLVDH FNPYCPGKKQ SDEFKTALDR
VAILNKTGGT GRGMWSLRPG VE
//
